Metabolism of (+)-abscisic acid to (+)-7′-hydroxyabscisic acid by bromegrass cell cultures

Hampson, C.; Reaney, Martin J. T.; Abrams, Garth D.; Abrams, Suzanne R.; Gusta, L. V.

doi:10.1016/0031-9422(92)83603-v

Cited by 42 publications

(37 citation statements)

References 15 publications

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“…These enzymatic properties of CYP707A3 are quite consistent with those of ABA 89-hydroxylase activity found in the microsomes from suspension-cultured maize cells (Krochko et al, 1998;Cutler et al, 2000). Although in vivo feeding experiments (Lehmann and Schwenen, 1988;Loveys and Milborrow, 1991;Hampson et al, 1992;Balsevich et al, 1994) indicated the presence of 79-hydroxylation activity for both (1)-ABA and (ÿ)-ABA in various plant species, these activities were probably due to the catalysis of enzymes other than Figure 9. Expression patterns of CYP707As in response to stresses.…”

Section: Expression Patterns Of Cyp707a Family Genes In Arabidopsissupporting

confidence: 61%

“…Although (1)-79-hydroxy-ABA has been shown to be produced as a minor metabolite in some plant species (Lehmann and Schwenen, 1988;Loveys and Milborrow, 1991;Hampson et al, 1992), we did not detect (1)-79-hydroxy-ABA in our assay conditions. It has also been reported that (ÿ)-ABA, an enantiomer at C-19 of natural (1)-ABA, was metabolized by suspension-cultured maize cells to unnatural phaseic acid, (1)-PA, and (ÿ)-79-hydroxy-ABA (Balsevich et al, 1994).…”

Section: Characteristics Of the Reactionsmentioning

confidence: 46%

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Arabidopsis CYP707As Encode (+)-Abscisic Acid 8′-Hydroxylase, a Key Enzyme in the Oxidative Catabolism of Abscisic Acid

Saito

Hirai²,

Matsumoto³

et al. 2004

Plant Physiology

502

420

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Abscisic acid (ABA) is involved in a number of critical processes in normal growth and development as well as in adaptive responses to environmental stresses. For correct and accurate actions, a physiologically active ABA level is controlled through fine-tuning of de novo biosynthesis and catabolism. The hydroxylation at the 89-position of ABA is known as the key step of ABA catabolism, and this reaction is catalyzed by ABA 89-hydroxylase, a cytochrome P450. Here, we demonstrate CYP707As as the P450 responsible for the 89-hydroxylation of (1)-ABA. First, all four CYP707A cDNAs were cloned from Arabidopsis and used for the production of the recombinant proteins in insect cells using a baculovirus system. The insect cells expressing CYP707A3 efficiently metabolized (1)-ABA to yield phaseic acid, the isomerized form of 89-hydroxy-ABA. The microsomes from the insect cells exhibited very strong activity of 89-hydroxylation of (1)-ABA (K m ¼ 1.3 mM and k cat ¼ 15 min ÿ1 ). The solubilized CYP707A3 protein bound (1)-ABA with the binding constant K s ¼ 3.5 mM, but did not bind (ÿ)-ABA. Detailed analyses of the reaction products confirmed that CYP707A3 does not have the isomerization activity of 89-hydroxy-ABA to phaseic acid. Further experiments revealed that Arabidopsis CYP707A1 and CYP707A4 also encode ABA 89-hydroxylase. The transcripts of the CYP707A genes increased in response to salt, osmotic, and dehydration stresses as well as ABA. These results establish that the CYP707A family plays a key role in regulating the ABA level through the 89-hydroxylation of (1)-ABA.

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Section: Expression Patterns Of Cyp707a Family Genes In Arabidopsissupporting

confidence: 61%

Section: Characteristics Of the Reactionsmentioning

confidence: 46%

Arabidopsis CYP707As Encode (+)-Abscisic Acid 8′-Hydroxylase, a Key Enzyme in the Oxidative Catabolism of Abscisic Acid

Saito

Hirai²,

Matsumoto³

et al. 2004

Plant Physiology

502

420

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“…On the other hand, metabolism of (-)-ABA occurs through other catabolic pathways than (+)-ABA. For example, in bromegrass cell cultures (-)-ABA was transformed principally to (-)-7 -hydroxy ABA (Hampson et al 1992), while in tomato it was converted predominantly to (-)-ABA-GE (Vaughan and Milborrow 1984).…”

Section: Aba Metabolism In L Fendleri Suspension Cell Culturementioning

confidence: 99%

Abscisic acid metabolism and lipid accumulation of a cell suspension culture of Lesquerella fendleri

Kharenko

Zaharia

Giblin

et al. 2010

Plant Cell Tiss Organ Cult

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Lesquerella fendleri (commonly known as "Fendler's bladderpod" or "yellowtop") is a member of the Brassicaceae and is an important seed oil-producing plant. The lipid profile of L. fendleri seed indicates potential for producing a high quality replacement for castor oil. In this work, characterization of the lipid content of a suspension cell culture, derived from seedlings of L. fendleri, is provided. Under the described suspension cell culture conditions, 16:0, 18:1 9, 18:2 9, 12 and 18:3 9, 12, 15 fatty acids were found to accumulate in the cells, while 16:0, 26:0 and 28:0 fatty acids were predominant in the culture medium. Subsequently, the effect of application of abscisic acid (ABA), which modulates lipid accumulation, was assessed.

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“…ABA is also catabolized by the hydroxylation at C-7' and -9' of ABA to form 7'-and 9'-hydroxy ABAs, respectively (Hampson et al, 1992;Zhou et al, 2004). (-)-R-ABA, an ABA analog, is metabolized into (+)-phaseic acid in corn cell culture possibly by ABA 7'-hydroxylase (Balsevich et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

ABA 9′-hydroxylation is catalyzed by CYP707A in Arabidopsis

et al. 2011

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Abscisic acid (ABA) catabolism is important for regulating endogenous ABA levels. Neophaseic acid (neoPA) is one of the ABA catabolites produced via ABA 9'-hydroxylation, but the gene encoding ABA 9'-hydroxylase has not been identified. We found that endogenous neoPA levels reduced in loss-of-function mutants defective in ABA 8'-hydroxylase (CYP707A) genes. In addition, levels of both neoPA and PA reduced similarly when wild-type plants were treated with uniconazole-P, a P450 inhibitor. Furthermore, in vitro enzyme assay using microsomal fraction from yeast expressing CYP707A showed that all four Arabidopsis CYP707As contained both ABA 8'-and 9'-hydroxylase activities, although ABA 9'-hydroxylase activity is minor. These results demonstrate that ABA 9'-hydroxylation is catalyzed by CYP707A as a side reaction in Arabidopsis. Cover letterDear Editor, Please find enclosed our manuscript entitled "ABA 9'-hydroxylation is catalyzed by CYP707A in Arabidopsis". We would like to submit this manuscript for publication in the Phytochemistry. Abscisic acid (ABA) catabolism is important for regulating endogenous ABA levels in plant's response to environmental or developmental cues. ABA is catabolized through hydroxylation at either C-8', C-9', or C-7' and also through glycosylation. ABA 8'-hydroxyation is a key catabolic reaction, which is catalyzed by cytochrome P450 CYP707As. However, the gene coding ABA 9'-hydroxylases has not been identified. Here, we report that four Arabidopsis CYP707As catalyze both ABA 8'-and 9'-hydroxylation. This finding reveals the new enzymatic function of CYP707As, which ultimately helps to evaluate the role of each ABA catabolic pathway in other plant species in future.We would like to suggest expert reviewers for reviewing this manuscript. We hope that our manuscript is acceptable for publication in the Phytochemistry.We look forward to hearing from you.Sincerely, Masanori Okamoto & Eiji Nambara *Graphical Abstract Arabidopsis CYP707As catalyze both ABA 8'-and 9'-hydroxylation, but ABA 9'-hydroxylase activity is minor. Therefore, PA and neoPA are produced as major and minor catabolites of CYP707A, respectively. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 Title: *Research HighlightsABA 9'-hydroxylation is catalyzed by CYP707A in Arabidopsis AbstractAbscisic acid (ABA) catabolism is important for regulating endogenous ABA levels.Neophaseic acid (neoPA) is one of the ABA catabolites produced via ABA 9!-hydroxylation, but the gene encoding ABA 9!-hydroxylase has not been identified.We found that endogenous neoPA levels reduced in loss-of-function mutants defective in ABA 8!-hydroxylase (CYP707A) genes. In addition, levels of both neoPA and PA reduced similarly when wild-type plants were treated with uniconazole-P, a P450 inhibitor. Furthermore, in vitro enzyme assay using microsomal ...

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Metabolism of (+)-abscisic acid to (+)-7′-hydroxyabscisic acid by bromegrass cell cultures

Cited by 42 publications

References 15 publications

Arabidopsis CYP707As Encode (+)-Abscisic Acid 8′-Hydroxylase, a Key Enzyme in the Oxidative Catabolism of Abscisic Acid

Arabidopsis CYP707As Encode (+)-Abscisic Acid 8′-Hydroxylase, a Key Enzyme in the Oxidative Catabolism of Abscisic Acid

Abscisic acid metabolism and lipid accumulation of a cell suspension culture of Lesquerella fendleri

ABA 9′-hydroxylation is catalyzed by CYP707A in Arabidopsis

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